Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni.

Objective: Comamonas testosteroni Pb50 is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This bacterial strain is capable of utilizing phenol as the sole carbon and energy source. Although examples are known in which the C.

Isolation and partial characterization of catechol 1,2-dioxygenase of phenol degrading yeast Candida tropicalis.

Objectives: Candida tropicalis yeast is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This yeast is capable of utilizing phenol as the sole carbon and energy source. While the enzyme participating on the first step of phenol biodegradation, NADPH-dependent phenol hydroxylase, has already been characterized, information on the enzyme participating in the second step of its degradation, catechol 1,2-dioxygenase, is scarce.

Isolation of cytoplasmic NADPH-dependent phenol hydroxylase and catechol-1,2-dioxygenase from Candida tropicalis yeast.

The efficiencies of NADPH-dependent phenol hydroxylase (EC 1.14.13.